Abstract
Although many proteins have been found to exist as homooligomers in nature, t he biological significance and mechanism for its occurring is far from clear. We have examined a variety of proteins that exhibit homooligomerization and revealed that such a process of reversible protein-protein interaction can be utilized to effectively modulate the biological activities of proteins in responding to fluctuations of environmental conditions. A general mechanism for the disassembly and reassembly of such oligomeric proteins, needed for the transformation of their oligomeric states from one to another, appears to occur as such that the disassembly process occurs in a stepwise manner, while the reassembly occurs in a non-stepwise manner. The significance of the protein homo-oligomerization, an underappreciated phenomenon in the field of proteinprotein interactions, needs to be reappraised.
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